کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
8260157 | 1534656 | 2014 | 13 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Mahogunin ring finger 1 suppresses misfolded polyglutamine aggregation and cytotoxicity
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کلمات کلیدی
TSG101LAMP2ATBSTAIP4CMANedd4MGRN1Mahogunin Ring Finger-1PrPBAFHECT3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide - 3- (4،5-dimethylthiazol-2-yl) -2،5-difenyltetrazolium bromideChaperone-mediated autophagy - Autofagy متعهد ChaperoneMTT - MTTBafilomycin - بافیلومایسینBis(monoacylglycero)phosphate - بیس (monoacylglycero) فسفاتPolyglutamine disease - بیماری PolyglutamineHuntington disease - بیماری هانتینگتونParkinson's disease - بیماری پارکینسونAggregation - تجمعTris-buffered saline Tween-20 - تریس بافر Tween-20 سالینRing - حلقهCytotoxicity - سمیت سلولیInclusion bodies - مجازات شاملBMP - مدیریت فرایند کسب و کارPrion protein - پروتئین پریونTumor susceptibility gene 101 - ژن 101 حساسیت تومورreally interesting new gene - ژن جدید واقعا جالبChloroquine - کلروکین Protein quality control - کنترل کیفیت پروتئین
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
سالمندی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
Polyglutamine diseases are a family of inherited neurodegenerative diseases caused by the expansion of CAG repeats within the coding region of target genes. Still the mechanism(s) by which polyglutamine proteins are ubiquitinated and degraded remains obscure. Here, for the first time, we demonstrate that Mahogunin 21 ring finger 1 E3 ubiquitin protein ligase is depleted in cells that express expanded-polyglutamine proteins. MGRN1 co-immunoprecipitates with expanded-polyglutamine huntingtin and ataxin-3 proteins. Furthermore, we show that MGRN1 is predominantly colocalized and recruits with polyglutamine aggregates in both cellular and transgenic mouse models. Finally, we demonstrate that the partial depletion of MGRN1 increases the rate of aggregate formation and cell death, whereas the overexpression of MGRN1 reduces the frequency of aggregate formation and provides cytoprotection against polyglutamine-induced proteotoxicity. These observations suggest that stimulating the activity of MGRN1 ubiquitin ligase might be a potential therapeutic target to eliminate the cytotoxic threat in polyglutamine diseases.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease - Volume 1842, Issue 9, September 2014, Pages 1472-1484
Journal: Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease - Volume 1842, Issue 9, September 2014, Pages 1472-1484
نویسندگان
Deepak Chhangani, Nobuyuki Nukina, Masaru Kurosawa, Ayeman Amanullah, Vibhuti Joshi, Arun Upadhyay, Amit Mishra,